デオキシシチジンキナーゼ
WordNet
- an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
- a nucleoside component of DNA; composed of cytosine and deoxyribose (同)cytidine
- the basic unit of money in Papua New Guinea
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/04/28 09:31:19」(JST)
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Deoxycytidine kinase |
PDB rendering based on 1p5z. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1P5Z, 1P60, 1P61, 1P62, 2A2Z, 2A30, 2A7Q, 2NO0, 2NO1, 2NO6, 2NO7, 2NO9, 2NOA, 2QRN, 2QRO, 2ZI3, 2ZI4, 2ZI5, 2ZI6, 2ZI7, 2ZI9, 2ZIA, 3HP1, 3IPX, 3IPY, 3KFX, 3MJR, 3QEJ, 3QEN, 3QEO, 4JLK, 4L5B
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Identifiers |
Symbols |
DCK ; MGC117410; MGC138632 |
External IDs |
OMIM: 125450 MGI: 102726 HomoloGene: 616 ChEMBL: 2447 GeneCards: DCK Gene |
EC number |
2.7.1.74 |
Gene ontology |
Molecular function |
• deoxycytidine kinase activity
• ATP binding
• drug binding
• phosphotransferase activity, alcohol group as acceptor
• nucleoside kinase activity
• protein homodimerization activity
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Cellular component |
• nucleus
• cytosol
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Biological process |
• purine nucleobase metabolic process
• pyrimidine nucleobase metabolic process
• pyrimidine nucleotide metabolic process
• nucleotide biosynthetic process
• pyrimidine nucleoside salvage
• purine-containing compound salvage
• small molecule metabolic process
• nucleobase-containing small molecule metabolic process
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
1633 |
13178 |
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Ensembl |
ENSG00000156136 |
ENSMUSG00000029366 |
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UniProt |
P27707 |
P43346 |
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RefSeq (mRNA) |
NM_000788 |
NM_007832 |
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RefSeq (protein) |
NP_000779 |
NP_031858 |
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Location (UCSC) |
Chr 4:
71.86 – 71.9 Mb |
Chr 5:
88.76 – 88.78 Mb |
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PubMed search |
[1] |
[2] |
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Deoxycytidine kinase, also known as DCK, is an enzyme which in humans is encoded by the DCK gene.[1]
DCK transfers phosphate to deoxycytidine.
Contents
- 1 Function
- 2 See also
- 3 References
- 4 Further reading
- 5 External links
Function
Deoxycytidine kinase (DCK) is required for the phosphorylation of several deoxyribonucleosides and their nucleoside analogs. Deficiency of DCK is associated with resistance to antiviral and anticancer chemotherapeutic agents. Conversely, increased deoxycytidine kinase activity is associated with increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives. DCK is clinically important because of its relationship to drug resistance and sensitivity.[1]
See also
References
- ^ a b "Entrez Gene: DCK deoxycytidine kinase".
Further reading
- Hazra S, Szewczak A, Ort S, Konrad M, Lavie A (February 2011). "Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release". Biochemistry 50 (14): 2870–80. doi:10.1021/bi2001032. PMC 3071448. PMID 21351740.
- Hazra S, Konrad M, Lavie A (August 2010). "The sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analogs". J Med Chem 53 (15): 5792–800. doi:10.1021/jm1005379. PMC 2936711. PMID 20684612.
- Hazra S, Ort S, Konrad M, Lavie A (August 2010). "Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogs". Biochemistry 49 (31): 6748–90. doi:10.1021/bi100839e. PMC 2925221. PMID 20614893.
- Hazra S, Sabini E, Ort S, Konrad M, Lavie A (January 2009). "Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase". Biochemistry 48 (6): 1256–63. doi:10.1021/bi802062w. PMC 2701478. PMID 19159229.
- Sabini E, Hazra S, Konrad M, Lavie A (July 2008). "Elucidation of Different Binding Modes of Purine Nucleosides to Human Deoxycytidine Kinase". J. Med. Chem. 51 (14): 4219–25. doi:10.1021/jm800134t. PMC 2636677. PMID 18570408.
- Sabini E, Hazra S, Ort S, Konrad M, Lavie A (May 2008). "Structural basis for substrate promiscuity of dCK". J. Mol. Biol. 378 (3): 607–21. doi:10.1016/j.jmb.2008.02.061. PMC 2426910. PMID 18377927.
- McSorley T, Ort S, Hazra S, Lavie A, Konrad M (March 2008). "Mimicking phosphorylation of Ser-74 on human deoxycytidine kinase selectively increases catalytic activity for dC and dC analogues". FEBS Lett. 582 (5): 720–4. doi:10.1016/j.febslet.2008.01.048. PMC 2636680. PMID 18258203.
- Sabini E, Hazra S, Konrad M, Lavie A (June 2007). "The non-enantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with l- and d-nucleosides". J. Med. Chem. 50 (13): 3004–14. doi:10.1021/jm0700215. PMC 2586175. PMID 17530837.
- Sabini E, Hazra S, Konrad M, Burley SK, Lavie A (2007). "Structural basis for activation of the therapeutic l-nucleoside analogs 3TC and troxacitabine by human deoxycytidine kinase". Nucleic Acids Res. 35 (1): 186–92. doi:10.1093/nar/gkl1038. PMC 1802566. PMID 17158155.
- Arnér ES, Eriksson S (1996). "Mammalian deoxyribonucleoside kinases". Pharmacol. Ther. 67 (2): 155–86. doi:10.1016/0163-7258(95)00015-9. PMID 7494863.
- Chottiner EG, Shewach DS, Datta NS, et al. (1991). "Cloning and expression of human deoxycytidine kinase cDNA". Proc. Natl. Acad. Sci. U.S.A. 88 (4): 1531–5. doi:10.1073/pnas.88.4.1531. PMC 51053. PMID 1996353.
- Eriksson S, Cederlund E, Bergman T, et al. (1991). "Characterization of human deoxycytidine kinase. Correlation with cDNA sequences". FEBS Lett. 280 (2): 363–6. doi:10.1016/0014-5793(91)80332-W. PMID 2013338.
- Yamada Y, Goto H, Ogasawara N (1984). "Purine nucleoside kinases in human T- and B-lymphoblasts". Biochim. Biophys. Acta 761 (1): 34–40. PMID 6315069.
- Hurley MC, Palella TD, Fox IH (1984). "Human placental deoxyadenosine and deoxyguanosine phosphorylating activity". J. Biol. Chem. 258 (24): 15021–7. PMID 6317685.
- Spasokoukotskaja T, Arnér ES, Brosjö O, et al. (1995). "Expression of deoxycytidine kinase and phosphorylation of 2-chlorodeoxyadenosine in human normal and tumour cells and tissues". Eur. J. Cancer 31A (2): 202–8. doi:10.1016/0959-8049(94)00435-8. PMID 7718326.
- Stegmann AP, Honders MW, Bolk MW, et al. (1993). "Assignment of the human deoxycytidine kinase (DCK) gene to chromosome 4 band q13.3-q21.1". Genomics 17 (2): 528–9. doi:10.1006/geno.1993.1365. PMID 8406512.
- Song JJ, Walker S, Chen E, et al. (1993). "Genomic structure and chromosomal localization of the human deoxycytidine kinase gene". Proc. Natl. Acad. Sci. U.S.A. 90 (2): 431–4. doi:10.1073/pnas.90.2.431. PMC 45676. PMID 8421671.
- Johansson M, Brismar S, Karlsson A (1997). "Human deoxycytidine kinase is located in the cell nucleus". Proc. Natl. Acad. Sci. U.S.A. 94 (22): 11941–5. doi:10.1073/pnas.94.22.11941. PMC 23663. PMID 9342341.
- Hatzis P, Al-Madhoon AS, Jüllig M, et al. (1998). "The intracellular localization of deoxycytidine kinase". J. Biol. Chem. 273 (46): 30239–43. doi:10.1074/jbc.273.46.30239. PMID 9804782.
- Saada A, Shaag A, Mandel H, et al. (2001). "Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy". Nat. Genet. 29 (3): 342–4. doi:10.1038/ng751. PMID 11687801.
- Veuger MJ, Heemskerk MH, Honders MW, et al. (2002). "Functional role of alternatively spliced deoxycytidine kinase in sensitivity to cytarabine of acute myeloid leukemic cells". Blood 99 (4): 1373–80. doi:10.1182/blood.V99.4.1373. PMID 11830489.
- Innoceta A, Galluzzi L, Ruzzo A, et al. (2002). "Molecular basis of 2',3'-dideoxycytidine-induced drug resistance in human cells". Mol. Cell. Biochem. 231 (1–2): 173–7. doi:10.1023/A:1014441209108. PMID 11952160.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Krawiec K, Kierdaszuk B, Shugar D (2003). "Inorganic tripolyphosphate (PPP(i)) as a phosphate donor for human deoxyribonucleoside kinases". Biochem. Biophys. Res. Commun. 301 (1): 192–7. doi:10.1016/S0006-291X(02)03007-3. PMID 12535661.
- van der Wilt CL, Kroep JR, Loves WJ, et al. (2003). "Expression of deoxycytidine kinase in leukaemic cells compared with solid tumour cell lines, liver metastases and normal liver". Eur. J. Cancer 39 (5): 691–7. doi:10.1016/S0959-8049(02)00813-4. PMID 12628850.
- Ge Y, Jensen TL, Matherly LH, Taub JW (2004). "Physical and functional interactions between USF and Sp1 proteins regulate human deoxycytidine kinase promoter activity". J. Biol. Chem. 278 (50): 49901–10. doi:10.1074/jbc.M305085200. PMID 14514691.
- Usova E, Maltseva T, Földesi A, et al. (2005). "Human deoxycytidine kinase as a deoxyribonucleoside phosphorylase". J. Mol. Biol. 344 (5): 1347–58. doi:10.1016/j.jmb.2004.10.016. PMID 15561147.
- Mani RS, Usova EV, Eriksson S, Cass CE (2005). "Fluorescence studies of substrate binding to human recombinant deoxycytidine kinase". Nucleosides Nucleotides Nucleic Acids 23 (8–9): 1343–6. doi:10.1081/NCN-200027609. PMID 15571255.
PDB gallery
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1p5z: Structure of human dCK complexed with cytarabine and ADP-MG
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1p60: Structure of human dCK complexed with 2'-Deoxycytidine and ADP, Space group C 2 2 21
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1p61: Structure of human dCK complexed with 2'-Deoxycytidine and ADP, P 43 21 2 space group
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1p62: Structure of human dCK complexed with gemcitabine and ADP-MG
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2a2z: Crystal Structure of human deoxycytidine kinase in complex with deoxycytidine and uridine diphosphate
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2a30: Crystal structure of human deoxycytidine kinase in complex with deoxycytidine
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2a7q: Crystal structure of human dCK complexed with clofarabine and ADP
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2no9: The structure of deoxycytidine kinase complexed with troxacitabine and ADP.
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2noa: The structure of deoxycytidine kinase complexed with lamivudine and ADP.
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External links
- Deoxycytidine kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
Transferases: phosphorus-containing groups (EC 2.7)
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2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
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2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate
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2.7.3: N acceptor |
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2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
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2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
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2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
Polymerase |
DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
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RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
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Phosphorolytic
3' to 5' exoribonuclease |
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Uridylyltransferase |
- Glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
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Guanylyltransferase |
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Other |
- Recombinase (Integrase)
- Transposase
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2.7.8: miscellaneous |
Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
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Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
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2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
2.7.10: protein-tyrosine |
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2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
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2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
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2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Noninvasive detection of tumor-infiltrating T cells by PET reporter imaging.
- McCracken MN, Vatakis DN, Dixit D, McLaughlin J, Zack JA, Witte ON.
- The Journal of clinical investigation.J Clin Invest.2015 May 1;125(5):1815-26. doi: 10.1172/JCI77326. Epub 2015 Mar 30.
- Adoptive transfer of tumor-reactive T cells can successfully reduce tumor burden; however, in rare cases, lethal on-target/off-tumor effects have been reported. A noninvasive method to track engineered cells with high sensitivity and resolution would allow observation of correct cell homing and/or i
- PMID 25822024
- Deoxycytidine-kinase (dCK) knock-down as a novel myeloprotective strategy in the context of fludarabine, cytarabine, or cladribine therapy.
- Lachmann N1, Czarnecki K1, Brennig S1, Phaltane R1, Heise M1, Heinz N2, Kempf H3, Dilloo D4, Kaever V5, Schambach A6, Heuser M7, Moritz T1.
- Leukemia.Leukemia.2015 Apr 29. doi: 10.1038/leu.2015.108. [Epub ahead of print]
- PMID 25921248
- Methylation of IRAK3 is a novel prognostic marker in hepatocellular carcinoma.
- Kuo CC1, Shih YL1, Su HY1, Yan MD1, Hsieh CB1, Liu CY1, Huang WT1, Yu MH1, Lin YW1.
- World journal of gastroenterology : WJG.World J Gastroenterol.2015 Apr 7;21(13):3960-9. doi: 10.3748/wjg.v21.i13.3960.
- AIM: To examine the methylation levels of interleukin-1 receptor-associated kinase 3 (IRAK3) and GLOXD1 and their potential clinical applications in hepatocellular carcinoma (HCC).METHODS: mRNA expression and promoter methylation of IRAK3 and GLOXD1 in HCC cells were analyzed by reverse transcriptio
- PMID 25852282
Japanese Journal
- Twenty Novel Genetic Variations and Haplotype Structures of the DCK Gene Encoding Human Deoxycytidine Kinase (dCK)
- KIM Su-Ryang,SAITO Yoshiro,MAEKAWA Keiko,SUGIYAMA Emiko,KANIWA Nahoko,UENO Hideki,OKUSAKA Takuji,IKEDA Masafumi,MORIZANE Chigusa,YAMAMOTO Noboru,YOSHIDA Teruhiko,KAMATANI Naoyuki,FURUSE Junji,ISHII Hiroshi,SAIJO Nagahiro,OZAWA Shogo,SAWADA Jun-ichi
- Drug metabolism and pharmacokinetics 23(5), 379-384, 2008-10-25
- NAID 10024384731
- OP-355 Gemicitabine/Cisplatin併用療法の効果予測におけるdeoxycytidine kinase (dCK) mRNA量の可能性(膀胱腫瘍/薬物療法,一般演題口演,第96回日本泌尿器科学会総会)
- 丹司 望,尾澤 彰,柳原 豊,山口 晶子,西田 智保,池田 哲大,島本 憲司,青木 克徳,横山 雅好
- 日本泌尿器科學會雜誌 99(2), 360, 2008-02-20
- NAID 110006653694
Related Links
- Deoxycytidine kinase, also known as DCK, is an enzyme which in humans is encoded by the DCK gene. DCK transfers phosphate to deoxycytidine. Contents. 1 Function; 2 See also; 3 References; 4 Further reading; 5 External links ...
- 18 Apr 2012 ... Sequence or UniProt identifier. >sp|P27707|DCK_HUMAN Deoxycytidine kinase OS=Homo sapiens GN=DCK PE=1 SV=1 MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN ...
Related Pictures
★リンクテーブル★
[★]
キナーゼ カイネース リン酸化酵素 phosphoenzyme phosphotransferase
[★]
デオキシシチジン
- 関
- CdR、CDR、dC